ArticleNucleic acids research2016
High-temperature single-molecule kinetic analysis of thermophilic archaeal MCM helicases.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Single-molecule DNA-flow stretching assay as a versatile hybrid tool for investigating DNA-protein interactions.BMB reports · 2025Review
- The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024Review
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021Review
- Unwinding 20 Years of the Archaeal Minichromosome Maintenance Helicase.Journal of bacteriology · 2020Review
- The mechanism of DNA unwinding by the eukaryotic replicative helicase.Nature communications · 2019Article
- Diatrack particle tracking software: Review of applications and performance evaluation.Traffic (Copenhagen, Denmark) · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The minichromosome maintenance (MCM) complex is the replicative helicase responsible for unwinding DNA during archaeal and eukaryal genome replication. To mimic long helicase events in the cell, a high-temperature single-molecule assay was designed to quantitatively measure long-range DNA unwinding of individual DNA helicases from the archaeons Methanothermobacter thermautotrophicus (Mth) and Thermococcus sp. 9°N (9°N). Mth encodes a single MCM homolog while 9°N encodes three helicases. 9°N MCM3, the proposed replicative helicase, unwinds DNA at a faster rate compared to 9°N MCM2 and to Mth MCM. However, all three MCM proteins have similar processivities. The implications of these observations for DNA replication in archaea and the differences and similarities among helicases from different microorganisms are discussed. Development of the high-temperature single-molecule assay establishes a system to comprehensively study thermophilic replisomes and evolutionary links between archaeal, eukaryal, and bacterial replication systems.
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Registered trials
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